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Spectral Response of Hemoproteins to the Effect of Peroxidized Phosphatidylcholine and Its Derivatives
Abstract
Based on the analysis of spectral changes in 403–423 nm wavelength range of a number of heme-containing proteins (human hemoglobin, equine myoglobin, horseradish peroxidase and bovine cytochrome C), it was found that the effect of UV-irradiated phosphatidylcholine (or oleic acid), expressed in the development of a differential spectrum in the Soret band (ΔD) during their interaction, is characteristic for hemoproteins of both animal and plant origin. It was shown that the intensity of the spectral response under the specified conditions was distributed in the following order: peroxidase ≥ myoglobin ≥ hemoglobin ≥ cytochrome C. The determination of peroxidase as the best indicator for the detection of peroxidized lipids by the spectroscopic method can be used while conducting clinical and biochemical studies with its participation, as well as for the development of new methods for diagnosing the body’s protection ability against oxidative stress and predicting its ability to recover from diseases of varying severity.
About the Authors
N. M. Litvinko
Institute of Bioorganic Chemistry of the National Academy of Sciences of Belarus
Belarus
Belarus
Мinsk
D. O. Gerlovsky
Institute of Bioorganic Chemistry of the National Academy of Sciences of Belarus
Belarus
Belarus
Мinsk
L. A. Skorostetskaya
Institute of Bioorganic Chemistry of the National Academy of Sciences of Belarus
Belarus
Belarus
Мinsk
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Review
For citations:
Litvinko N.M., Gerlovsky D.O., Skorostetskaya L.A. Spectral Response of Hemoproteins to the Effect of Peroxidized Phosphatidylcholine and Its Derivatives. Zhurnal Prikladnoii Spektroskopii. 2025;92(6):784-792. (In Russ.)
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